The Researcher's Guide to Measuring Binding Affinity and Why It Matters

The Researcher’s Guide to Measuring Binding Affinity and Why It Matters About this eBook

Find out the key principles for measuring binding affinity, including the critical parameters to consider and what solutions are available. Whether you’re just starting to learn about binding interactions or you want a refresher, this guide will provide helpful tips to better understand, evaluate, and eventually purchase the best technology for your needs. Contents

What is binding affinity?...... 1 Why measure binding affinity?...... 2 When do researchers measure binding affinity?...... 3 What tools are available to measure binding affinity?...... 4 Technologies for measuring binding affinity...... 9 How do I evaluate my research needs?...... 9 How can I find the right solution?...... 10 How do I evaluate vendors?...... 11 How do I make an informed decision?...... 13 How do I acquire the technology?...... 13 Total cost of investment...... 15 Buyer’s checklist...... 16 Resources for binding affinity...... 17 What is binding affinity? While it's very common for biologists and chemists to test whether or not two molecules interact with each other, it's much more useful to gather information on the nature of that interaction. How strong is it? How long will it last? What does this mean for its biological function? These questions can be answered by studying binding affinity.

Binding affinity is the strength of the interaction between a single biomolecule and its binding partner, or ligand. It can be quantified, providing information on whether or not molecules are interacting as well as assigning a value to the affinity.

Typically, when measuring binding affinity, you’re interested in several parameters, but mostly in the unit

of measurement called the dissociation constant (Kd), which defines the likelihood that an interaction between two molecules will break. The smaller the dissociation constant, the more tightly bound the ligand is and the higher the affinity is between the two molecules.

“The dissociation constant (Kd ) defines the likelihood that an interaction between two molecules will break and is a useful measurement to quantify binding affinity.”

Binding affinity is an important metric used in both academia and industry. Academic researchers study binding affinity to learn about structural biology, structure-function relationships, and the intermolecular interactions that drive biological processes. On the other hand, drug developers study binding affinity to identify high-affinity molecules that bind to drug targets selectively and specifically. In this case, affinity can guide decisions about the biological relevance of a particular molecule, such as whether the molecule under investigation warrants further screening or characterization.

1 Why measure binding affinity?

Almost every process in biology can be attributed to an interaction between molecules. With the thousands of individual molecules that make up a cell, researchers are challenged with determining which types of molecules interact with each other and figuring out the consequences of these interactions.

Scientists use Kd to determine or “rank-order” binding reactions that may often translate into biological function or uncover the relevance of the targets being examined. The more researchers know about these interactions, the more they understand the biological systems in which they work with their intricate network of molecular pathways that control various cellular processes.

Precisely characterizing biomolecular interactions in a biological system is an important cornerstone in basic research. In applied science, measuring the binding affinity of interactions is a prerequisite for the development of new products, such as drugs, enzymes or biomarkers. Measuring binding affinity has many applications, including identifying and screening small and/or large molecules, monitoring the regulation of cellular pathways, screening compound and drug candidates, testing structure-function relationships, and optimizing the development of assays that examine the interaction of two molecules.

2 “Precisely characterizing biomolecular interactions in a biological system is an important cornerstone in basic research.”

When do researchers measure binding affinity? Now that you understand the what and why of binding affinity, it’s time to discuss when it comes into play in the research workflow. Primarily, when you are interested in finding out if two molecules interact in a pathway or process of interest, you use binding affinity assays to see how they interact or bind to each other.

You can also measure binding affinity when modifying a molecule as a way to see how changing its binding properties relates to the pathway or process you are studying. Binding affinity is also useful when you need MEASURING BINDING AFFINITY IS USEFUL FOR: to develop a functional assay to monitor a pathway, • Characterizing receptor binding properties as you may need to measure binding as part of the assay. • Measuring interactions with antibodies • Analyzing protein complexes Academic researchers typically want to understand • Investigating enzyme inhibition the biology and regulation of a target molecule that • Observing molecular transport processes may or may not have any therapeutic potential. For • Mapping epitopes example, to understand a molecular pathway, it is • Optimizing leads important to be able to selectively modify molecules • Pursuing fragment-based lead discovery and quantitatively determine how these modifications • Measuring the effects of buffers, solutions, and concentration influence the overall pathway. on binding affinity

On the industry side of the research spectrum, binding affinity is a useful metric during the earliest parts of the drug development process when scientists are screening for any compounds that interact with their target of interest. Beginning with a large library of compounds or ligands, industry scientists begin the screening process by identifying which ones bind to the target protein, and then continue with an increasingly smaller pool of compound candidates. After they complete much of their pre-clinical work, researchers may measure binding affinity to determine and rank various compounds’ binding affinities for the target protein as an indicator of potency of a possible drug candidate. What tools are available to measure binding affinity? QUALITY COUNTS When it comes to measuring binding affinity, or performing Scientists use many different tools to measure binding any other experiment, for that matter, the quality of your affinity, although most of them fall into one of two results will depend on the quality of the source material. categories: qualitative methods and quantitative methods. If you don’t have any data on the quality of your source Qualitative methods such as ELISAs, pull-down assays, material, the experiment is less likely to succeed. and gel shift assays work by immobilizing one protein to a substrate and applying another protein (typically containing a label or reporter tag) to it. If the two proteins bind, they release a detectable signal. These methods merely provide a yes/no answer as to whether binding occurred. These techniques may be suitable for labs that occasionally analyze protein interactions or are examining protein interactions at a very gross level.

In contrast, quantitative methods provide a scalar readout of binding affinity, releasing a signal that indicates the strength of the interaction. Biosensor-based methodologies work by immobilizing a binding partner to a surface and presenting the test partner to interact with it. The change in signal is observed and recorded by the instrument. Other quantitative methods use capillaries or tubes instead of immobilizing proteins to a surface.

In this section, we’ll walk through the most common biophysical technologies and their strengths and weaknesses in terms of throughput, speed, sensitivity, and ease of use.

4 Surface Plasmon Resonance

Surface plasmon resonance (SPR) is a common Strengths Additionally, SPR measures changes in biosensor-based technique for measuring SPR determines binding kinetics and refractive index. Any buffer component that biomolecular interactions. constants using label-free detection, which influences the refractive index of a sample eliminates the need for dyes and tags and (e.g. DMSO, a common solvent for small How it works allows for higher-sensitivity measurements. molecules) can cause artifacts in SPR SPR is a surface-based biosensor reporting This method also conserves lab resources by measurements. Usually, control experiments technology. It requires the immobilization of one consuming low volumes of sample. are necessary when working with DMSO. binding partner, the ligand. The other binding Finally, because SPR depends on mass partner, the analyte, is injected into a flow cell Weaknesses changes on the chip surface, this technology and comes into contact with the ligand on the Immobilization of the ligand is not always is not an optimal solution for small molecule surface at a constant flow rate. The interaction of straightforward. Although diverse chip- research. ligand and analyte leads to an increase in mass surfaces, coupling chemistries and even bound to the surface, which results in a signal specific chips are available, some ligands Conclusion change. The signal is plotted in resonance units cannot be immobilized in a functional way. SPR is a highly sensitive and precise tool that (RU) (also referred to as response units). The This is especially important in small molecule provides kinetic and affinity data. Considered resulting sensograms display an association research, where capture antibodies cannot a gold standard for both academic and phase which depends on the association rate be used (to avoid unspecific binding to the industry research applications, it has many constant (kon), followed by a dissociation phase antibody). Many “difficult” targets, such as established standard protocols. However, (only buffer is pumped through the flow cell) membrane proteins, are fragile and do not it can be costly and a bit complicated to which depends on the dissociation rate constant tolerate the acidic surface of the SPR assay. operate, and is not suited as a walk-up (k ). By testing different analyte concentrations instrument in a dynamic research setting. off Also, for interactions where the analyte does presented to a constant amount of immobilized not wash off easily, scientists must identify ligand, the k , k and K of the interaction can on off d regeneration conditions that can break be determined. the ligand-analyte interaction to facilitate dissociation but leave the ligand intact for another binding experiment.

5 Isothermal Titration Calorimetry

Isothermal titration calorimetry (ITC) is partner as the absorption or production of Moreover, the buffers in the sample cell and considered the most quantitative technique heat is an intrinsic property of virtually all syringe have to be identical, which is typically available for measuring the thermodynamic biochemical reactions. In addition, ITC can be achieved by dialysis overnight. Discrepancies properties of interactions. used to measure affinity and stoichiometry, and between the buffers results in additional signals is the only technique in this list to enable direct which preclude a precise analysis of the data. How it works determination of thermodynamics (ΔH, ΔS). ITC is a calorimetric method which measures Another constraint of ITC is the low binding-induced heat changes. For this, a Weaknesses throughput. One titration typically takes 30 to sample in-solution is placed into a sample cell, ITC requires large quantities of sample. 60 minutes, so the throughput is limited to ~20 and water is placed into a reference cell. Both Any miniaturization of the instrument to 40 Kds per day (with the automated version cells are kept at exactly the same temperature. would require a massive improvement in taking up to 24 hours). Then, titrating amounts of the binding partner sensitivity, which is technically challenging Because no single-use consumables are used, are added into the sample cell while stirring. since the heat changes are so small. Also, the instrument needs trained personnel to The energy required to keep the cells at since one always works at concentrations take care of regular washing and maintenance identical temperatures is measured, meaning above the K , the amount of target in d of the sample cells and syringes. Replacement that the heat released or absorbed due to a the sample cell has to be quite high. In of broken components can be costly and time- binding event results in a measurable signal. addition, the concentration of the ligand consuming. This signal becomes smaller with increasing in the syringe used to introduce one of the occupancy of the target molecule. From the binding partners must be extremely high, Conclusion data, one can calculate Kd, stoichiometry, and especially when investigating rather weak ITC is often considered the “gold standard” binding thermodynamics (ΔH, ΔS). interactions (in the higher μM range). This for label-free protein binding analysis. In is often difficult to achieve for many protein Strengths contrast to SPR, it is truly label-free, since preparations, or simply may exceed the it does not require any modification of the This technique relies upon the accurate solubility of the ligand because the volume interaction partners. However, it’s not suited measurement of heat changes that result from per injection is small (1-5 μL). for high-throughput screening because of the the interaction of molecules in solution. There large amounts of sample required and long is no need to label or immobilize either binding titration times.

6 BioLayer Interferometry

BioLayer Interferometry (BLI) is a label-free Strengths Especially for high-affinity interactions, the technology for measuring biomolecular Its ease of use and throughput make it mass-transfer-limitation is an important factor, interactions. an attractive option, especially for labs as well as the limitation in measurement times

developing mAb. Kinetic analysis (kon, koff) due to sample evaporation from the plate. How it works and analysis of affinity can also be performed. BLI is an optical biosensor-based technique Measurements are fast as it is a "dip and Conclusion that analyzes the interference pattern of white Although BLI is less sensitive than SPR, read" methodology. light reflected from two surfaces: a layer of it’s easier to use. It’s a great tool for mAb immobilized protein on the biosensor tip, and Weaknesses development workflows. There are options an internal reference layer. Any change in the BLI is a less sensitive and less robust method for low, medium and higher throughput number of molecules bound to the biosensor than SPR, which makes it poorly suited for sample analysis. tip causes a shift in the interference pattern applications examining small-molecule that can be measured in real-time, providing interaction partners. This, however, does detailed information regarding the kinetics not apply for most mAb applications. of association and dissociation of the two As with SPR, a covalent coupling of molecules as well as the affinity constant biomolecules is difficult and faces the same for the interaction (k , k and K ). Due to on off d hurdles in terms of immobilization conditions. the biosensor tip design, the technique is Moreover, it is hardly possible to achieve highly amenable to both purified and crude identical ligand coatings of multiple biosensor samples as well as high throughput screening tips, so that regeneration of a tip is still experiments. The detection method can also required if concentration series are measured. be used to determine the molar concentration of analytes.

7 MicroScale Thermophoresis

MicroScale thermophoresis (MST) free, and analysis can be done in any specific buffer conditions, or for looking at quantitatively examines molecular buffer including complex bioliquids, thus interactions in close-to-native conditions. interactions in solution at the microliter scale. examination occurs in close-to-native A label-free option is available. Because there It measures binding interactions utilizing the conditions. The strength of the interactions are minimal moving parts and nothing needs characteristics of thermophoresis combined between a fluorescently labeled sample (or to be cleaned, MST can be considered with Temperature Related Intensity Change intrisically fluorescent sample) and a binding a maintenance-free instrument. (TRIC). Thermophoresis is the movement of partner (or ligand) are measured while a molecules in the presence of a thermal gradient microscopic temperature gradient, induced Weaknesses Absolute binding kinetic constants (K and K ) and TRIC is the quenching of a fluorophore by an infrared laser, is applied over time. The off on can not be identified with MST. While there are when subjected to a thermal gradient. Thus, resulting MST signal is detected and plotted label-free options, fluorescent labeling of one MST is influenced by a molecule’s size, charge, against the ligand concentration to obtain a of the binding partners is typically required to hydration shell and the effects of TRIC. dose-response curve, from which the binding perform an analysis. Altogether, the data generated results in a affinity (Kd) is automatically calculated. precise and robust measurement of binding Strengths Conclusion interactions and modifications. The method MST is the most versatile, rapid and easy- It is an in-solution method in which binding works equally well in standard buffers and to-use method and can precisely measure partners being studied are not immobilized biological liquids like blood or cell-lysate. MST binding affinity for virtually every type of on a biosensor or solid surface. With this provides information regarding the binding biomolecular interaction. It has been shown technology, binding affinity is determined affinity (K ) of two or more interacting proteins. to obtain results on difficult targets that are d using very small amounts of sample. Results challenging to evaluate by other binding How it works are measured in minutes. It’s also very flexible, affinity methods. MST is performed in-solution in thin, glass meaning you can look at molecules of all capillaries that hold low, microliter volumes weights and in all sorts of buffers — ideal for of sample. The method is immobilization- investigating sensitive molecules that need

8 Technologies for measuring binding affinity Isothermal Surface Plasmon Titration BioLayer MicroScale Resonance Calorimetry Interferometry Thermophoresis (SPR) (ITC) (BLI) (MST)

Requires high amount of sample No Yes No No

Label-free Yes Yes Yes Optional

Immobilization-free No Yes No Yes

High throughput Yes No Yes Yes

Easy to use No No Yes Yes

Instrument costs High Low Medium Medium

Consumable costs High Low Medium Medium

Measures binding kinetics Yes No Yes No

How do I evaluate my research needs? If you’ve determined that you need an instrument that can measure binding affinity, there are some simple steps you can take to find out which one would be right for your lab. Sometimes, just the thought of purchasing new technology can be overwhelming—it can be a costly and significant decision for your lab. But you can make the process much easier for yourself by taking the time to think about your needs and how the instrument could fit into your established workflow. What are your research or project goals? What is most important to you? What are your

9 biggest challenges and bottlenecks in your workflow? Setting costs and budgets aside for a moment, think about what you need in terms of throughput, speed, sensitivity, robustness and precision of data.

Be sure to not only think about the immediate needs of HOW CAN I FIND THE RIGHT SOLUTION? your lab, but also consider what you plan to work on in Once you have a better idea of what you need, it’s time to the foreseeable future. For example, today, you may be start searching for information about the various solutions interested in protein-DNA interactions, but in a few months, available. In addition to reading through this guide, there your research may expand to include G-protein-coupled- are many ways to do your due diligence so you can make as receptors. Your work is most important and may require educated a decision as possible. flexible technology that can support it for years to come. When you are evaluating a platform for its flexibility, ask the vendor if the platform’s hardware and software can be upgraded. This way, you will get the most from your system TO LEARN ABOUT TECHNOLOGIES THAT MEASURE today and in the years to come. BINDING AFFINITY, YOU CAN: • Visit scientific websites Additionally, you may want to choose an instrument you will • Visit vendor websites use frequently because it makes your workflow more efficient, • Visit online blogs and forums thereby saving you a lot of time and money. Finally, consider • Ask colleagues the ease-of-use of the technology, since instruments that are • Visit vendor booths at conferences too complicated to use are often abandoned by the laboratory • Attend a webinar staff once the expert user leaves. • Call sales representatives • Look at advertisements and articles in journals (online and print) • Listen to the chatter on social media channels “Choose an instrument you will use • Explore scientific groups frequently because it makes your workflow more efficient, thereby saving you a lot of time and money.”

10 Analyzing binding affinity can get complicated, you may even need to consider adopting multiple technologies to tackle your research. You could, for example, use a faster VENDORS (ALPHA ORDER) technology that requires less sample to filter out 80% of the molecules in your sample, and then use a slow, more complex method to further study the remaining 20%. ForteBio www.fortebio.com The approach of using a faster, less complicated ForteBio makes Octet and BLItz, instruments technology will save you time, effort and money and for BioLayer Interferometry allow you to focus on the most relevant targets that will further your research.

GE Healthcare Life Sciences www.proteins.gelifesciences.com How do I The Biacore Series from GE uses Surface Plasmon Resonance evaluate vendors? Several vendors offer technologies for measuring binding affinity, and you can find most of the information about Malvern Instruments their product offerings on their websites or in sales www.malverninstruments.com collateral such as catalogs, brochures, and videos. Malvern’s MicroCal instruments enable Isothermal Titration Calorimetry You can help yourself answer fundamental questions about the features of the platform you are considering by browsing the product specifications and features, NanoTemper Technologies such as whether or not the instrument and software are www.nanotempertech.com user-friendly, the size of the system's footprint, and what NanoTemper offers Monolith, a series of consumables are required for its use. products for MicroScale Thermophoresis

Although this information will certainly help, it may not answer all of your questions. Therefore, you may need to contact the vendor. Before you do that, you may want to

11 prepare a list of questions that will help you determine if the solution is right for your lab. These might include: Are the consumables complicated to use? How easy is it to collect data? Does the platform require training to operate? What types of upgrades are available? Does it have the throughput I need?

Remember, you’re looking for solutions that solve problems tied directly to your research goals. A lot of technologies boast cutting-edge features that sound impressive but are not practical for everyday use. Instead of letting those extra bells and whistles influence your decision, stay focused on only the attributes that matter to your research.

For a third-party perspective, you could ask colleagues in the research community what instruments they use. Scan through peer-reviewed research that used the technology and determine if the platform can address your research challenges. You could also read reviews online to see what is recommended. At this stage, it’s important to gather as much information as possible about each technology’s benefits and drawbacks.

When you purchase a piece of equipment, you are starting an ongoing relationship with a Pro Tip vendor. When purchasing a platform, scientists often overlook the step of vetting the vendor’s reputation and credibility in the industry. Questions to ask include: How long has the company been around? How many customers do they have? Are they global? Am I served by a local representative? What kind of support do they offer, and are customers satisfied with the support they receive? In other words, will this company be with me when I run into problems? What’s their response time, and how active will they be in solving my problem?

The most reliable source for this type of information comes from 1) talking with colleagues who have experience with that vendor, and 2) reading product reviews generated by customers. Tap into your network to learn about a company’s reputation.

This information will help you decide which vendor offers the best solution for your lab.

12 How do I make an informed decision? Based on the information you find by researching potential solutions and their manufacturers, you should be able to narrow down your list to one or two choices. You may want to ask vendors for a product demo so you can see how their systems work on your samples. In fact, their response can be a good indication of how easy their product is to set up and run. If the demo can be done quickly and without much difficulty, you can imagine how easy it will be to integrate it into your workflow.

Use the demo as an opportunity to put these products to the test. Don’t just test them yourself — let the other researchers in your lab run samples on the system and provide feedback. Then, you will have a few more data points to further support your decision.

“You may want to ask vendors for a product demo so you can see how their systems work on your samples. In fact, their response can be a good indication of how easy their product is to set up and run.”

How do I acquire the technology?

Once you have made a final selection, you are ready to begin the process of acquiring a new technology. You can embark on this endeavor by yourself, or you can work with a contract research organization, a collaborator, a vendor, or through a core facility to incorporate the technology into your workflow.

13 Buying a new instrument is not often a decision you make alone. There is usually a committee Pro Tip or group in place who must weigh in. An essential part of the buying process is figuring out who the stakeholders are and what they need to know so you can supply them with the right information.

In most cases, a lab manager or procurement officer is responsible for the budget. He or she will likely want to know that you’ve evaluated your options and that you are choosing the best instrument for the job. Engage these decision-makers early and often. You will end up presenting them with multiple quotes and options before all is said and done, so it’s good to get their input before expecting to receive their full buy-in.

Also influencing the decision is anyone who will be using the instrument. Generally, your colleagues’ top concerns will include making sure the software and instrument are easy to use, that it doesn’t slow down their work, and that it is easy to train others to use it. These influencers may also want to evaluate the instrument’s technical capabilities to make sure it can give them the data they want.

If you are the person taking the lead on purchasing the equipment for your lab, the first question to ask is: How much it will cost? Some offerings include the product only, but others may include the product as well as the software, and in some cases, they’ll include consumables, too. To get a sense of the total cost of investment, including upfront and ongoing costs, ask vendors what is included and not included in the quote they give you.

Next, you will need to figure out a way to pay for it. Your institution may already have a plan in place for purchasing new capital equipment, in which case you may be able to use money that has been set aside previously. Alternatively, you can factor in your new equipment purchase as part of a new budget for the following year. Depending on how the purchasing process works at your organization, you may need to involve a lab manager or procurement officer. Find out what kind of documentation you need to provide to gain approval.

14 Your funding source for new equipment will vary depending on if you are in academia or industry. At a university, you TOTAL COST OF INVESTMENT can apply for a grant to fund the purchase. Also, you may Budgeting properly for a new instrument means looking receive support from external sources that are interested at more than just the price tag––there are other costs to in funding your research. These external sources include consider. Here is everything to be aware of when thinking foundations, private donations, crowdsourcing platforms such about the total cost of your investment: as GoFundMe, or collaborations with other groups that have similar interests. • Purchasing costs – the sticker price of the new system • Installation costs – how much it costs to have the To make the purchase more affordable, consider asking for instrument set up by the vendor support from other groups at your institution who share your • Running costs – how much it costs to run the system interests and have extra funding. Or, consider purchasing an in terms of consumables and energy entry-level instrument and plan to upgrade it at a later time. • Service and maintenance costs – how much you will get charged for repairs or regularly scheduled maintenance, As with any other big purchases, once the financing is in and how that impacts lab downtime place, the rest of the process is relatively straightforward. • Support costs – how much it will cost to get technical Most technologies will require some form of installation, support for the software or scientific support for your implementation, and training. Aside from occasional support applications and maintenance, your new instrument is ready to become • Additional software upgrades – what you can expect an invaluable part of your workflow, providing valuable data to pay for major software upgrades that supports your research.

15 Buyer’s Checklist

Here are questions to ask as you’re going through the buying process. Step 3: Evaluate vendors • Look at their credibility in the research community Step 1: Explore your research needs • Are there many publications that use this solution? • What challenge(s) am I facing? How recent are they, and are they in relevant journals that • Is there a solution available? promote high-quality research? • Who or which labs have their instrument? Step 2: Explore available solutions • What do felllow researchers recommend? • Does the solution solve my challenge(s)? • How long has the company been around? »» What are the benefits of the solution? • How many customers do they have? Does that fit what I need now, in the near future, later? • Are they global? • What types of solutions are available? • What kind of support do they offer? »» Am I getting the instrument only, the instrument and software, • Am I served by a local representative? or the instrument, software and consumables? »» Is support included? Step 4: Make an informed decision »» Is service included? • Compare the different technologies side-by-side • What is important to consider when selecting a solution? • Narrow to a few choices »» Is the instrument user-friendly? • Ask a sales rep questions »» Is the software user-friendly? • Ask for a demo »» Are the consumables complicated to use? • Verify the solution fits the need »» How easy is it to collect data? »» Does the instrument have a small footprint? Step 5: Purchase the technology »» Does it require training to operate? • How much will it cost? »» What types of upgrades are available? • What’s included in the cost? »» Does it have the throughput I need? • How am I going to pay for it? • Who is responsible in the buying decision? • Will others be using the technology? • What information do they need to know?

16 Conclusion As a researcher, chances are a critical piece of your experiments involves knowing how a protein interacts with other molecules. By measuring binding affinity, you can gain new insights into those interactions and what they mean. Now that you’re informed about what binding affinity is and how it works, you will know how to identify, evaluate and purchase the appropriate tools or technologies for your lab.

Resources for Binding Affinity If you are interested in learning more about binding affinity and other bioanalytical screening methods, visit these resources:

LinkedIn Groups Community Forums and Focus Groups Analytical & Bioanalytical Chemistry (ABC) American Association of Pharmaceutical Scientists https://www.linkedin.com/groups/1822503/profile https://www.aaps.org/Bioanalytical/

Bioanalytical Method Development Bioanalysis Zone https://www.linkedin.com/groups/4229880/profile https://www.bioanalysis-zone.com/

Bioanalytical Solutions Peer-Reviewed Journal Articles https://www.linkedin.com/groups/2458704/profile “A Guide to Simple and Informative Binding Assays” http://www.molbiolcell.org/content/21/23/4061.full Clinical/Nonclinical Bioanalytical and PK Consultants https://www.linkedin.com/groups/1334367/profile “On the Binding Affinity of Macromolecular Interactions: Daring to Ask Why Proteins Interact” NanoTemper Bioanalytics User Group https://www.ncbi.nlm.nih.gov/pmc/articles/ https://www.linkedin.com/groups/4482307 PMC3565702/

17 When proteins matter. NanoTemper’s mission is to enable researchers to do the best science of their lives

NanoTemper Technologies is deeply committed to the best customer experience. Central to this is a strong focus on enabling researchers to easily, efficiently, and accurately perform protein characterization. With a broad offering of systems, software and consumables for evaluating binding affinities, protein stability and protein quality, scientists in pharmaceutical, biotech or academic labs will find an optimized workflow, quality results and responsive customer support. Work with a deeply experienced and globally operating team, and realize the NanoTemper experience.

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